Water retention capabilities of collagen, gelatin and peptide as studied by IR/QCM/RH system.Spectrochim Acta A Mol Biomol Spectrosc. 2020 Jun 19; 241:118619.SA
In this study, water retention properties of triple helix collagen, gelatin (separated single chains) and peptide (broken peptide fragments) were studied by using IR micro-spectroscopy equipped with a relative humidity (RH) control system and quartz crystal microbalance (QCM). Adsorbed water ratios (wt%) are found to be in the order of collagen, gelatin and peptide (at about RH = 60%, 22 wt% for collagen, 14 wt% for gelatin and 9 wt% for peptide). Free water molecules with longer H bonds are the major adsorbed water species for collagen, gelatin and peptide. IR band shifts and changes in normalized band areas of functional groups are generally larger for collagen than gelatin and peptide, indicating larger interactions of water molecules with functional groups such as aliphatic CH2, CH3, amides, COO- and C-O for collagen. Relations between normalized band areas show that water molecules are interacting with aliphatic CH species and C-O bonds of collagen. Since the fibril structures of collagen triple helices are reported to be cross-linked by sugars, water molecules can be attracted to polar C-O bonds of sugars linking collagen triple helices in fibrils and they are interacting with adjacent aliphatic CH side chains on the surface of fibrils.